ID   F0NLS4_SULIH            Unreviewed;       400 AA.
AC   F0NLS4;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 53.
DE   RecName: Full=2-oxoacid oxidoreductase (ferredoxin) {ECO:0000256|ARBA:ARBA00012691};
DE            EC=1.2.7.11 {ECO:0000256|ARBA:ARBA00012691};
GN   OrderedLocusNames=SiH_2505 {ECO:0000313|EMBL:ADX83842.1};
OS   Sulfolobus islandicus (strain HVE10/4).
OC   Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=930943 {ECO:0000313|EMBL:ADX83842.1, ECO:0000313|Proteomes:UP000006395};
RN   [1] {ECO:0000313|EMBL:ADX83842.1, ECO:0000313|Proteomes:UP000006395}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HVE10/4 {ECO:0000313|EMBL:ADX83842.1,
RC   ECO:0000313|Proteomes:UP000006395};
RX   PubMed=21278296; DOI=10.1128/JB.01487-10;
RA   Guo L., Brugger K., Liu C., Shah S.A., Zheng H., Zhu Y., Wang S.,
RA   Lillestol R.K., Chen L., Frank J., Prangishvili D., Paulin L., She Q.,
RA   Huang L., Garrett R.A.;
RT   "Genome analyses of icelandic strains of Sulfolobus islandicus, model
RT   organisms for genetic and virus-host interaction studies.";
RL   J. Bacteriol. 193:1672-1680(2011).
CC   -!- FUNCTION: Catalyzes the coenzyme A-dependent oxidative decarboxylation
CC       of different 2-oxoacids such as 2-oxoglutarate, pyruvate and 2-
CC       oxobutyrate to form their CoA derivatives.
CC       {ECO:0000256|ARBA:ARBA00003908}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2-oxocarboxylate + CoA + 2 oxidized [2Fe-2S]-[ferredoxin] =
CC         an acyl-CoA + CO2 + H(+) + 2 reduced [2Fe-2S]-[ferredoxin];
CC         Xref=Rhea:RHEA:42316, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:33737,
CC         ChEBI:CHEBI:33738, ChEBI:CHEBI:35179, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:58342; EC=1.2.7.11;
CC         Evidence={ECO:0000256|ARBA:ARBA00000005};
CC   -!- SUBUNIT: Heterodimer composed of an alpha and a beta subunit.
CC       {ECO:0000256|ARBA:ARBA00011631}.
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DR   EMBL; CP002426; ADX83842.1; -; Genomic_DNA.
DR   RefSeq; WP_012716784.1; NC_017275.1.
DR   AlphaFoldDB; F0NLS4; -.
DR   GeneID; 8762715; -.
DR   KEGG; sih:SiH_2505; -.
DR   HOGENOM; CLU_002569_5_0_2; -.
DR   Proteomes; UP000006395; Chromosome.
DR   GO; GO:0018491; F:2-oxobutyrate synthase activity; IEA:UniProt.
DR   GO; GO:0047553; F:2-oxoglutarate synthase activity; IEA:UniProt.
DR   GO; GO:0019164; F:pyruvate synthase activity; IEA:UniProt.
DR   CDD; cd07034; TPP_PYR_PFOR_IOR-alpha_like; 1.
DR   Gene3D; 3.40.50.920; -; 1.
DR   Gene3D; 3.40.50.970; -; 1.
DR   InterPro; IPR033412; PFOR_II.
DR   InterPro; IPR002880; Pyrv_Fd/Flavodoxin_OxRdtase_N.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR009014; Transketo_C/PFOR_II.
DR   PANTHER; PTHR32154:SF30; 2-OXOACID OXIDOREDUCTASE (FERREDOXIN); 1.
DR   PANTHER; PTHR32154; PYRUVATE-FLAVODOXIN OXIDOREDUCTASE-RELATED; 1.
DR   Pfam; PF17147; PFOR_II; 1.
DR   Pfam; PF01855; POR_N; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
DR   SUPFAM; SSF52922; TK C-terminal domain-like; 1.
PE   4: Predicted;
KW   Pyruvate {ECO:0000313|EMBL:ADX83842.1}.
FT   DOMAIN          15..237
FT                   /note="Pyruvate flavodoxin/ferredoxin oxidoreductase
FT                   pyrimidine binding"
FT                   /evidence="ECO:0000259|Pfam:PF01855"
FT   DOMAIN          263..363
FT                   /note="Pyruvate:ferredoxin oxidoreductase core"
FT                   /evidence="ECO:0000259|Pfam:PF17147"
SQ   SEQUENCE   400 AA;  44717 MW;  ED06B568B1BEEBD0 CRC64;
     MIRKIISGNE AVALGVKLAR VGVTGIYPIT PQTTIIEKLA EMRAKGEIET EIVRVESEHS
     AMAATFGAAL GGVRAFTATA SQGLLYMHEM IWWVAGSRVP VVMVVGTRAV GAPWNIWNEH
     TDFTSERDSG WIMAFASNPQ EALDLTLQAF RISEDERVFL PMMVGMDGFI LSHTKTNVLI
     PDQDQVDEFL PPRRQPYVID PEDPIGMGNI FPPEGYMRLR ESIDLALRNS ENIIKEIGRE
     YNKKINPLGD YSTLNVSYKL EDADYAIVLM GAWAGDAMEA VDTLREKGIK IGMLRIRYLR
     PWSEKEIRNA LKDKRAVLVL DRSTSFGRGG GPLYVEVKST ISDIVPQVKG VVSGLGGVTV
     NKSELLYIFN KFVEGLKDDV IWYYPKEVGK IEFRTPRDIE
//